Synthesis and antipepsin activities of peptides having a valine or valylvaline moiety at the N-terminus.

Publisher Website
Google Scholar
Abstract
A series of peptides having a valine or valylvaline moiety at the N-terminus, was prepared and their antipepsin activities were tested. All of the peptides possessing an N-acyl-Val-Val moiety, except 1, showed some inhibitor activity against pepsin, while compounds lacking N-acyl-Val-Val showed no inhibition even at a concentration of 50 .mu.g/ml. A pepstatin [Actinomycete product] analog, in which a tyrosine residue is present instead of AHMHA [4-amino-3-hydroxy-6-methyl heptanoic acid] of pepstatins, was the most potent inhibitor among the synthetic peptides, but its activity was markedly lower than that of pepstatin A. Some compounds showed neither agonistic nor antagonistic effects on pepstatin A, suggesting major differences in binding abilities of the synthetic peptides and of pepstatin A to the enzyme. The importance of the AHMHA residue of pepstatins in relation to the inhibitory activity is discussed.

This publication has 1 reference indexed in Scilit: